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Protein

Glutathione S-transferase A4

Gene

Gsta4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91GlutathioneBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_215316. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase A4 (EC:2.5.1.18)
Alternative name(s):
GST A4-4
Short name:
GSTA4-4
GST class-alpha member 4
Glutathione S-transferase 5.7
Short name:
GST 5.7
Gene namesi
Name:Gsta4
Synonyms:Gsta
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1309515. Gsta4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Glutathione S-transferase A4PRO_0000185791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP24472.
PaxDbiP24472.
PRIDEiP24472.

2D gel databases

REPRODUCTION-2DPAGEP24472.

PTM databases

PhosphoSiteiP24472.

Expressioni

Gene expression databases

BgeeiP24472.
CleanExiMM_GSTA4.
GenevestigatoriP24472.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP24472. 2 interactions.
MINTiMINT-1487605.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94Combined sources
Turni14 – 163Combined sources
Helixi17 – 2610Combined sources
Beta strandi31 – 344Combined sources
Helixi38 – 458Combined sources
Turni46 – 483Combined sources
Beta strandi50 – 534Combined sources
Beta strandi57 – 604Combined sources
Beta strandi63 – 653Combined sources
Helixi68 – 7811Combined sources
Helixi86 – 10823Combined sources
Helixi109 – 1113Combined sources
Helixi114 – 13118Combined sources
Helixi133 – 14210Combined sources
Beta strandi145 – 1528Combined sources
Helixi155 – 16814Combined sources
Helixi174 – 1774Combined sources
Helixi179 – 18911Combined sources
Helixi192 – 1987Combined sources
Beta strandi199 – 2035Combined sources
Helixi210 – 21910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B48X-ray2.60A/B2-222[»]
1GUKX-ray2.90A/B1-222[»]
ProteinModelPortaliP24472.
SMRiP24472. Positions 2-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24472.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8381GST N-terminalAdd
BLAST
Domaini85 – 208124GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 552Glutathione binding
Regioni67 – 682Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG266414.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiP24472.
KOiK00799.
OMAiVLRMYYD.
OrthoDBiEOG79CZ0K.
PhylomeDBiP24472.
TreeFamiTF105321.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24472-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAKPKLYYF NGRGRMESIR WLLAAAGVEF EEEFLETREQ YEKMQKDGHL
60 70 80 90 100
LFGQVPLVEI DGMMLTQTRA ILSYLAAKYN LYGKDLKERV RIDMYADGTQ
110 120 130 140 150
DLMMMIAVAP FKTPKEKEES YDLILSRAKT RYFPVFEKIL KDHGEAFLVG
160 170 180 190 200
NQLSWADIQL LEAILMVEEL SAPVLSDFPL LQAFKTRISN IPTIKKFLQP
210 220
GSQRKPPPDG PYVEVVRTVL KF
Length:222
Mass (Da):25,564
Last modified:January 23, 2002 - v3
Checksum:iB580E3415289424D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361E → D in BAB31640. (PubMed:16141072)Curated
Sequence conflicti205 – 2062KP → SA in BAB27873. (PubMed:16141072)Curated
Sequence conflicti218 – 2181T → I in AAA37754. (PubMed:1426286)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151K → P Requires 2 nucleotide substitutions.
Natural varianti167 – 1671V → G.
Natural varianti179 – 1802PL → GE.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06047 mRNA. Translation: AAA37754.1.
AK008189 mRNA. Translation: BAB25520.1.
AK008193 mRNA. Translation: BAB25524.1.
AK008400 mRNA. Translation: BAB25649.1.
AK008490 mRNA. Translation: BAB25696.1.
AK009668 mRNA. Translation: BAB26429.1.
AK010098 mRNA. Translation: BAB26701.1.
AK011177 mRNA. Translation: BAB27449.1.
AK011841 mRNA. Translation: BAB27873.1.
AK019100 mRNA. Translation: BAB31546.1.
AK019271 mRNA. Translation: BAB31640.1.
BC012639 mRNA. Translation: AAH12639.1.
CCDSiCCDS23357.1.
PIRiS27234.
RefSeqiNP_034487.2. NM_010357.3.
UniGeneiMm.2662.

Genome annotation databases

EnsembliENSMUST00000034903; ENSMUSP00000034903; ENSMUSG00000032348.
GeneIDi14860.
KEGGimmu:14860.
UCSCiuc009qty.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06047 mRNA. Translation: AAA37754.1.
AK008189 mRNA. Translation: BAB25520.1.
AK008193 mRNA. Translation: BAB25524.1.
AK008400 mRNA. Translation: BAB25649.1.
AK008490 mRNA. Translation: BAB25696.1.
AK009668 mRNA. Translation: BAB26429.1.
AK010098 mRNA. Translation: BAB26701.1.
AK011177 mRNA. Translation: BAB27449.1.
AK011841 mRNA. Translation: BAB27873.1.
AK019100 mRNA. Translation: BAB31546.1.
AK019271 mRNA. Translation: BAB31640.1.
BC012639 mRNA. Translation: AAH12639.1.
CCDSiCCDS23357.1.
PIRiS27234.
RefSeqiNP_034487.2. NM_010357.3.
UniGeneiMm.2662.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B48X-ray2.60A/B2-222[»]
1GUKX-ray2.90A/B1-222[»]
ProteinModelPortaliP24472.
SMRiP24472. Positions 2-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP24472. 2 interactions.
MINTiMINT-1487605.

PTM databases

PhosphoSiteiP24472.

2D gel databases

REPRODUCTION-2DPAGEP24472.

Proteomic databases

MaxQBiP24472.
PaxDbiP24472.
PRIDEiP24472.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034903; ENSMUSP00000034903; ENSMUSG00000032348.
GeneIDi14860.
KEGGimmu:14860.
UCSCiuc009qty.2. mouse.

Organism-specific databases

CTDi2941.
MGIiMGI:1309515. Gsta4.

Phylogenomic databases

eggNOGiNOG266414.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiP24472.
KOiK00799.
OMAiVLRMYYD.
OrthoDBiEOG79CZ0K.
PhylomeDBiP24472.
TreeFamiTF105321.

Enzyme and pathway databases

ReactomeiREACT_215316. Glutathione conjugation.

Miscellaneous databases

EvolutionaryTraceiP24472.
NextBioi287101.
PROiP24472.
SOURCEiSearch...

Gene expression databases

BgeeiP24472.
CleanExiMM_GSTA4.
GenevestigatoriP24472.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A subgroup of class alpha glutathione S-transferases. Cloning of cDNA for mouse lung glutathione S-transferase GST 5.7."
    Zimniak P., Eckles M.A., Saxena M., Awasthi Y.C.
    FEBS Lett. 313:173-176(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Small intestine and Tongue.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Characterization of a novel glutathione S-transferase isoenzyme from mouse lung and liver having structural similarity to rat glutathione S-transferase 8-8."
    Medh R.D., Saxena M., Singhal S.S., Ahmad H., Awasthi Y.C.
    Biochem. J. 278:793-799(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 106-120 AND 167-184.
    Strain: CD-1.
    Tissue: Liver and Lung.
  5. "Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress."
    Krengel U., Schroter K.H., Hoier H., Arkema A., Kalk K.H., Zimniak P., Dijkstra B.W.
    FEBS Lett. 422:285-290(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
    Tissue: Lung.
  6. "Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface."
    Xiao B., Singh S.P., Nanduri B., Awasthi Y.C., Zimniak P., Ji X.
    Biochemistry 38:11887-11894(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
    Tissue: Lung.

Entry informationi

Entry nameiGSTA4_MOUSE
AccessioniPrimary (citable) accession number: P24472
Secondary accession number(s): Q9CQ81
, Q9CTY7, Q9CY87, Q9D038
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2002
Last modified: January 7, 2015
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

On the basis of immunological and kinetics data, GST 5.7 is distinct from alpha, mu and pI classes of GTS. However it has been postulated that this protein may be part of a distinct subgroup within this alpha class.
The variations were found from AA sequencing and imply there are multiple forms of this protein. These variations are likely to be sex-linked and tissue specific.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.